A1D9Z6 (DCL2_NEOFI) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Dicer-like protein 2

Including the following 2 domains:

1. Endoribonuclease dcl2
   EC=3.1.26.-
2. ATP-dependent helicase dcl2
   EC=3.6.4.-

Gene names

Name:	dcl2
ORF Names:	NFIA_030600

Organism

Neosartorya fischeri (strain ATCC 1020 / DSM 3700 / FGSC A1164 / NRRL 181) (Aspergillus fischerianus) [Complete proteome]

Taxonomic identifier

331117 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Fungi › Dikarya › Ascomycota › saccharomyceta › Pezizomycotina › leotiomyceta › Eurotiomycetes › Eurotiomycetidae › Eurotiales › Trichocomaceae › Neosartorya › Neosartorya fischeri group › Neosartorya fischeri

Protein attributes

Sequence length	1388 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Function	Dicer-like endonuclease involved in cleaving double-stranded RNA in the RNA interference (RNAi) pathway. Produces 21 to 25 bp dsRNAs (siRNAs) which target the selective destruction of homologous RNAs leading to sequence-specific suppression of gene expression, called post-transcriptional gene silencing (PTGS). Part of a broad host defense response against viral infection and transposons By similarity.
Cofactor	Magnesium or manganese By similarity.
Sequence similarities	Belongs to the helicase family. Dicer subfamily. Contains 1 Dicer dsRNA-binding fold domain. Contains 1 helicase ATP-binding domain. Contains 1 helicase C-terminal domain. Contains 2 RNase III domains.

Ontologies

Keywords
Biological process	Antiviral defense
Domain	Repeat
Ligand	ATP-binding Magnesium Manganese Metal-binding Nucleotide-binding RNA-binding
Molecular function	Antiviral protein Helicase Hydrolase
Technical term	Complete proteome
Gene Ontology (GO)
Biological_process	RNA processing Inferred from electronic annotation. Source: InterPro defense response to virus Inferred from electronic annotation. Source: UniProtKB-KW regulation of defense response to virus Inferred from electronic annotation. Source: UniProtKB-KW
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW ATP-dependent helicase activity Inferred from electronic annotation. Source: InterPro RNA binding Inferred from electronic annotation. Source: UniProtKB-KW metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW ribonuclease III activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 1388	1388	Dicer-like protein 2		PRO_0000306795
Regions
	Domain	23 – 203	181	Helicase ATP-binding
	Domain	371 – 537	167	Helicase C-terminal
	Domain	564 – 658	95	Dicer dsRNA-binding fold
	Domain	919 – 1059	141	RNase III 1
	Domain	1098 – 1281	184	RNase III 2
	Nucleotide binding	36 – 43	8	ATP By similarity
	Motif	144 – 147	4	DEAH box
Sites
	Metal binding	1137	1	Magnesium or manganese By similarity
	Metal binding	1267	1	Magnesium or manganese By similarity
	Metal binding	1270	1	Magnesium or manganese By similarity
	Site	1263	1	Important for activity By similarity

Sequences

	Sequence		Length	Mass (Da)
	A1D9Z6 [UniParc]. Last modified January 23, 2007. Version 1. Checksum: C30E206A2EB2D3DB	FASTA	1,388	156,430
	10 20 30 40 50 60 MASSVTACQG ASPYQPRNYQ LEMLEASMKE NIIVAMDTGS GKTHIAVLRI KAELDICPPD 70 80 90 100 110 120 KLVWFLAPTV ALCIQQHEVI ASNLPAVRTR TLTGLDKVEL WTEQSIWDAV LNGYRVIVST 130 140 150 160 170 180 HAVLADALSH GFVKMSRLAL LIFDEAHHCT RRHAANKIMR DFYHPTLTKS GPGAVPRIMG 190 200 210 220 230 240 LTASPVVRSN HQELLTVESN LDAVCRTPRV HRQELVKFTH RPHLQQIWYT PTDPAGFKSA 250 260 270 280 290 300 SQTLGALYHA WETLDIGDDP YIQRLRKSPL DDTALKKALL TGKTYCREQL RRFVDRSRHI 310 320 330 340 350 360 FEELGEWAAE YYIYASIKQL GDRVRNSYMS GDWDEAEKAY LVDFLSKIPA SEIQLALNDP 370 380 390 400 410 420 GSFRISPKFE SLLNFLDSLD EREFSGLIFV KQRATVSAMT SLLSVHPCTR ERFRCAAYVG 430 440 450 460 470 480 WSNGSASKDI LGDLLNMQLQ RDTLDDFRSG RKNLIIATDV LEEGIDISAC SVVVCYDKPP 490 500 510 520 530 540 NLKSFVQRRG RARRKQSTFA IMFPTDDASA DVSKWQDLEQ AMIEAYQDDE RQLQSVSALE 550 560 570 580 590 600 SLDEEVMERL TVESTSAVLT ADMAMAHLHH FCAVLPPQPY ADMRPVFSFE TNEDGLLKGT 610 620 630 640 650 660 VILPSCVHPK VRRTEGRRWW RTERAAMKET AFQAYKALYE FGLVNDHLLP LTKRPELKSH 670 680 690 700 710 720 DLGAMPSILE TSEQYDPWIE WAYSWSSPDI HQSRIVVRMN EGRGDELCMR LMGPTYLPPL 730 740 750 760 770 780 SPMTLFWNNS TTFTVTFEAA ERVPLVPLSS VEDMRAITAL YLKATNSRVC SSERDFTALF 790 800 810 820 830 840 APDLHHTELK GWLNAYEGCD PAMEVYSRGH NPLLMGVVRD HSRYGEPFLF RKWLVSDQNP 850 860 870 880 890 900 SCSVVELECA PFPHRRNLLH RQRLANSQVD VDEETPESAA KNPIVAADAC TIDRLPFTMA 910 920 930 940 950 960 IFGLFISAIV ERLETELIAT RLRETILRDV GFKSTDHIIT AISTPFAHAL TNYQRYEFLG 970 980 990 1000 1010 1020 DSILKFSVSC QLFFQHPNWH EGYLSEGRAM IVQNPRLAKA ALDTGLDAYI VTKRIASRKW 1030 1040 1050 1060 1070 1080 SAPLISEKLE RVPAKRQMST KVLADVVEAL IGAAYMDGGH ATAQACIRRL LPEINLHAVD 1090 1100 1110 1120 1130 1140 TRTATRSVAP ESARHMMNER LKDHIGYTFE DESLLVEALT HPSCDYDSTT QSYQRLEYLG 1150 1160 1170 1180 1190 1200 DAVLDMVIVS AIFNHPIQRP QGDMTKIKHA VVNANLLAFL CMESATSEEK LDVAQTSKDS 1210 1220 1230 1240 1250 1260 FAVTTSQESV ELWRFMRYRG QNLNAARDAS LARHRALRDE IASSLLHAPH YPWHALSRLN 1270 1280 1290 1300 1310 1320 ADKFFSDIVE SVLGAIFVDS GGDLAPCEVF VERIGLMAYL RRILDQEIDV RHPRSVAQQL 1330 1340 1350 1360 1370 1380 AKTNIQFVLQ RVPNEEGGAS YQCSVRIEQA ELFVVTGCLT AEEAEVTAAV EAIKFLTRDE GSTPLNTS

References

[1]

"Genomic islands in the pathogenic filamentous fungus Aspergillus fumigatus." Fedorova N.D., Khaldi N., Joardar V.S., Maiti R., Amedeo P., Anderson M.J., Crabtree J., Silva J.C., Badger J.H., Albarraq A., Angiuoli S., Bussey H., Bowyer P., Cotty P.J., Dyer P.S., Egan A., Galens K., Fraser-Liggett C.M. , Haas B.J., Inman J.M., Kent R., Lemieux S., Malavazi I., Orvis J., Roemer T., Ronning C.M., Sundaram J.P., Sutton G., Turner G., Venter J.C., White O.R., Whitty B.R., Youngman P., Wolfe K.H., Goldman G.H., Wortman J.R., Jiang B., Denning D.W., Nierman W.C. PLoS Genet. 4:E1000046-E1000046(2008) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 1020 / DSM 3700 / FGSC A1164 / NRRL 181.

Cross-references

Sequence databases
EMBL GenBank DDBJ	DS027693 Genomic DNA. Translation: EAW20627.1.
RefSeq	XP_001262524.1. XM_001262523.1.
3D structure databases
ProteinModelPortal	A1D9Z6.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	CADNFIAT00002760; CADNFIAP00002683; CADNFIAG00002760.
GeneID	4589127.
KEGG	nfi:NFIA_030600.
Phylogenomic databases
eggNOG	COG1111.
HOGENOM	HOG000048683.
OrthoDB	EOG4JWZNK.
Family and domain databases
Gene3D	1.10.1520.10. 2 hits.
InterPro	IPR005034. Dicer_dsRNA_binding_fold. IPR011545. DNA/RNA_helicase_DEAD/DEAH_N. IPR014001. Helicase_ATP-bd. IPR001650. Helicase_C. IPR027417. P-loop_NTPase. IPR000999. RNase_III_dom. [Graphical view]
Pfam	PF00270. DEAD. 1 hit. PF03368. dsRNA_bind. 1 hit. PF00271. Helicase_C. 1 hit. PF00636. Ribonuclease_3. 2 hits. [Graphical view]
SMART	SM00487. DEXDc. 1 hit. SM00490. HELICc. 1 hit. SM00535. RIBOc. 2 hits. [Graphical view]
SUPFAM	SSF69065. RNase_III. 2 hits. SSF52540. SSF52540. 1 hit.
PROSITE	PS51327. DICER_DSRBF. 1 hit. PS51192. HELICASE_ATP_BIND_1. 1 hit. PS51194. HELICASE_CTER. 1 hit. PS00517. RNASE_3_1. 1 hit. PS50142. RNASE_3_2. 2 hits. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

DCL2_NEOFI

Accession

Primary (citable) accession number: A1D9Z6

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 2, 2007
Last sequence update:	January 23, 2007
Last modified:	May 29, 2013
This is version 42 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program